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Q8VI36

- PAXI_MOUSE

UniProt

Q8VI36 - PAXI_MOUSE

Protein

Paxillin

Gene

Pxn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).By similarity

    GO - Molecular functioni

    1. BH4 domain binding Source: MGI
    2. protein binding Source: IntAct
    3. receptor signaling complex scaffold activity Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. branching morphogenesis of an epithelial tube Source: MGI
    3. cellular component movement Source: MGI
    4. cytoskeleton organization Source: MGI
    5. focal adhesion assembly Source: MGI
    6. integrin-mediated signaling pathway Source: MGI
    7. lamellipodium assembly Source: MGI
    8. peptidyl-tyrosine phosphorylation Source: MGI
    9. positive regulation of protein kinase activity Source: MGI
    10. regulation of cell shape Source: MGI
    11. substrate adhesion-dependent cell spreading Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_206286. GAB1 signalosome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Paxillin
    Gene namesi
    Name:Pxn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:108295. Pxn.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcell cortex 1 Publication
    Note: Colocalizes with integrins at the cell periphery.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell leading edge Source: MGI
    3. cytoskeleton Source: UniProtKB-SubCell
    4. focal adhesion Source: MGI
    5. lamellipodium Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591PaxillinPRO_0000075854Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei31 – 311Phosphotyrosine; by PTK6By similarity
    Modified residuei83 – 831Phosphoserine2 Publications
    Modified residuei88 – 881Phosphotyrosine2 Publications
    Modified residuei106 – 1061PhosphoserineBy similarity
    Modified residuei118 – 1181Phosphotyrosine; by PTK64 Publications
    Modified residuei119 – 1191PhosphoserineBy similarity
    Modified residuei126 – 1261PhosphoserineBy similarity
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei137 – 1371PhosphoserineBy similarity
    Modified residuei181 – 1811PhosphotyrosineBy similarity
    Modified residuei244 – 2441Phosphoserine; by CDK5By similarity
    Modified residuei322 – 3221PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation By similarity. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8VI36.
    PaxDbiQ8VI36.
    PRIDEiQ8VI36.

    PTM databases

    PhosphoSiteiQ8VI36.

    Miscellaneous databases

    PMAP-CutDBQ8VI36.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VI36.
    BgeeiQ8VI36.
    CleanExiMM_PXN.
    GenevestigatoriQ8VI36.

    Interactioni

    Subunit structurei

    Interacts with VCL and SRC (via SH3 domain). Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 and PDCD10 By similarity. Interacts with SORBS1, PARVA and PARVB. Interacts with NEK3 and this interaction is prolactin-dependent By similarity. Interacts with PTK2/FAK1. Interacts with PTK6 By similarity. Interacts with PTK2B/PYK2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    L1camP116272EBI-983394,EBI-397964
    Ptk2P341523EBI-983394,EBI-77070
    PTPN1P180312EBI-983394,EBI-968788From a different organism.
    VclQ647273EBI-983394,EBI-432047

    Protein-protein interaction databases

    BioGridi202525. 16 interactions.
    IntActiQ8VI36. 20 interactions.
    MINTiMINT-141924.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VI36.
    SMRiQ8VI36. Positions 357-590.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini356 – 41560LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini416 – 47358LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini474 – 53360LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini534 – 59158LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 1513LD motif 1Add
    BLAST
    Motifi144 – 15613LD motif 2Add
    BLAST
    Motifi216 – 22813LD motif 3Add
    BLAST
    Motifi265 – 27612LD motif 4Add
    BLAST
    Motifi333 – 34513LD motif 5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi46 – 538Pro-rich

    Sequence similaritiesi

    Belongs to the paxillin family.Curated
    Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG267887.
    GeneTreeiENSGT00740000114891.
    HOGENOMiHOG000018764.
    HOVERGENiHBG001512.
    InParanoidiQ8VI36.
    KOiK05760.
    OrthoDBiEOG70ZZQN.
    PhylomeDBiQ8VI36.

    Family and domain databases

    Gene3Di2.10.110.10. 4 hits.
    InterProiIPR001904. Paxillin.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 4 hits.
    [Graphical view]
    PRINTSiPR00832. PAXILLIN.
    SMARTiSM00132. LIM. 4 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Beta (identifier: Q8VI36-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP    50
    PPPSSEALNG TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT 100
    QDGVGSLCSR AGEEEHVYSF PNKQKSAEPS PTVMSSSLGS NLSELDRLLL 150
    ELNAVQHSPP GFPADEAESS PPLPGALSPL YGIPENNTPL GGKAGPLVKE 200
    KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS 250
    SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR 300
    QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV 350
    ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD 400
    GQPYCEKDYH SLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF 450
    GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF 500
    VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM 550
    AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C 591
    Length:591
    Mass (Da):64,476
    Last modified:March 1, 2002 - v1
    Checksum:iB41A1892E6F60544
    GO
    Isoform Alpha (identifier: Q8VI36-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-311: Missing.

    Show »
    Length:557
    Mass (Da):60,811
    Checksum:i483D880CF16289B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711P → R in BAE42452. (PubMed:16141072)Curated
    Sequence conflicti212 – 2121D → N in BAE34151. (PubMed:16141072)Curated
    Sequence conflicti294 – 2941G → S in BAE34151. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei278 – 31134Missing in isoform Alpha. 2 PublicationsVSP_016357Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF293883 mRNA. Translation: AAL71910.1.
    AF293882 mRNA. Translation: AAL71909.1.
    AK149933 mRNA. Translation: BAE29176.1.
    AK157688 mRNA. Translation: BAE34151.1.
    AK167299 mRNA. Translation: BAE39404.1.
    AK171436 mRNA. Translation: BAE42452.1.
    CCDSiCCDS19593.1. [Q8VI36-2]
    CCDS39229.1. [Q8VI36-1]
    RefSeqiNP_035353.1. NM_011223.3. [Q8VI36-2]
    NP_598676.2. NM_133915.3.
    UniGeneiMm.18714.

    Genome annotation databases

    EnsembliENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528. [Q8VI36-2]
    GeneIDi19303.
    KEGGimmu:19303.
    UCSCiuc008zeb.1. mouse. [Q8VI36-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF293883 mRNA. Translation: AAL71910.1 .
    AF293882 mRNA. Translation: AAL71909.1 .
    AK149933 mRNA. Translation: BAE29176.1 .
    AK157688 mRNA. Translation: BAE34151.1 .
    AK167299 mRNA. Translation: BAE39404.1 .
    AK171436 mRNA. Translation: BAE42452.1 .
    CCDSi CCDS19593.1. [Q8VI36-2 ]
    CCDS39229.1. [Q8VI36-1 ]
    RefSeqi NP_035353.1. NM_011223.3. [Q8VI36-2 ]
    NP_598676.2. NM_133915.3.
    UniGenei Mm.18714.

    3D structure databases

    ProteinModelPortali Q8VI36.
    SMRi Q8VI36. Positions 357-590.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202525. 16 interactions.
    IntActi Q8VI36. 20 interactions.
    MINTi MINT-141924.

    PTM databases

    PhosphoSitei Q8VI36.

    Proteomic databases

    MaxQBi Q8VI36.
    PaxDbi Q8VI36.
    PRIDEi Q8VI36.

    Protocols and materials databases

    DNASUi 19303.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067268 ; ENSMUSP00000069624 ; ENSMUSG00000029528 . [Q8VI36-2 ]
    GeneIDi 19303.
    KEGGi mmu:19303.
    UCSCi uc008zeb.1. mouse. [Q8VI36-2 ]

    Organism-specific databases

    CTDi 5829.
    MGIi MGI:108295. Pxn.

    Phylogenomic databases

    eggNOGi NOG267887.
    GeneTreei ENSGT00740000114891.
    HOGENOMi HOG000018764.
    HOVERGENi HBG001512.
    InParanoidi Q8VI36.
    KOi K05760.
    OrthoDBi EOG70ZZQN.
    PhylomeDBi Q8VI36.

    Enzyme and pathway databases

    Reactomei REACT_206286. GAB1 signalosome.

    Miscellaneous databases

    ChiTaRSi PXN. mouse.
    NextBioi 296261.
    PMAP-CutDB Q8VI36.
    PROi Q8VI36.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VI36.
    Bgeei Q8VI36.
    CleanExi MM_PXN.
    Genevestigatori Q8VI36.

    Family and domain databases

    Gene3Di 2.10.110.10. 4 hits.
    InterProi IPR001904. Paxillin.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 4 hits.
    [Graphical view ]
    PRINTSi PR00832. PAXILLIN.
    SMARTi SM00132. LIM. 4 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes."
      Chay K.O., Park S.S., Mushinski J.F.
      J. Biol. Chem. 277:14521-14529(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
      Strain: BALB/c.
      Tissue: Testis.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
      Strain: C57BL/6J and NOD.
      Tissue: Placenta and Spleen.
    3. "The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells."
      Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A., Sattler M., Avraham H., Griffin J.D.
      J. Biol. Chem. 271:31222-31226(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B/PYK2, SUBCELLULAR LOCATION.
    4. "Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells."
      Ku H., Meier K.E.
      J. Biol. Chem. 275:11333-11340(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK1/ERK2.
    5. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
      Nikolopoulos S.N., Turner C.E.
      J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARVA.
    6. "The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin."
      Hayashi I., Vuori K., Liddington R.C.
      Nat. Struct. Biol. 9:101-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-88 AND TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway."
      Kopecki Z., O'Neill G.M., Arkell R.M., Cowin A.J.
      J. Invest. Dermatol. 131:1450-1459(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-118.

    Entry informationi

    Entry nameiPAXI_MOUSE
    AccessioniPrimary (citable) accession number: Q8VI36
    Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3